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J Gen Virol. 2015 Feb;96(Pt 2):277-87. doi: 10.1099/vir.0.069914-0. Epub 2014 Nov 4.

RIG-I from waterfowl and mammals differ in their abilities to induce antiviral responses against influenza A viruses.

Author information

1
State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, No. 2 Yuan Ming Yuan West Road, Beijing 100193, PR China.
2
State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, No. 2 Yuan Ming Yuan West Road, Beijing 100193, PR China lzdws@cau.edu.cn.

Abstract

The retinoic acid-induced gene I (RIG-I) plays a crucial role in sensing viral RNA and IFN-β production. RIG-I varies in length and sequence between different species. We assessed the functional differences between RIG-I proteins derived from mammals and birds. The transfection of duck caspase recruitment domains (CARDs) and duck RIG-I (dCARDs and dRIG-I) and goose CARDs and goose RIG-I (gCARDs and gRIG-I) into chicken DF-1 cells increased the production of IFN-β mRNA and IFN-stimulated genes and decreased influenza A virus (IAV) replication; whereas human CARDs and RIG-I (hCARDs and hRIG-I) and mouse CARDs and RIG-I (mCARDs and mRIG-I) had no effect. In human 293T and A549 cells, hCARDs had the strongest IFN-inducing activity, followed by mCARDs, dCARDs and gCARDs. The IFN-inducing activity of hRIG-I was stronger than that of mRIG-I, dRIG-I and gRIG-I, in that order. The results showed that, although the ability of dCARDs to activate IFN was stronger than that of gCARDs in DF-1, 293T and A549 cells, dRIG-I had a weaker ability to activate IFN than gRIG-I in DF-1 cells with or without IAV infection. These data suggest that RIG-I proteins from different species have different amino acid sequences and functions. This genetic and functional diversity renders RIG-I flexible, adaptable and capable of recognizing many viruses in different species.

PMID:
25371516
DOI:
10.1099/vir.0.069914-0
[Indexed for MEDLINE]

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